报告人：林圣彩 教授

　　厦门大学生命科学学院

　　报告时间: 2016年3月18日 星期五 上午10:00-11:30

　　报告地点：中科院大连化物所 生物楼一楼学术报告厅

　　报告人简介：

　　林圣彩 教授

　　长江学者特聘教授, 国家杰出青年基金获得者，国家重大科学研究计划项目首席科学家，中国生物化学与分子生物学学会副理事长，入选科技部“2012年度中国科学十大进展; 2013年度CCTV科技创新人物”评选中，被推选为“创新成果引领未来方向”17人之一.

　　1984年毕业于厦门大学生物系,获学士学位;1991年于美国西南医学中心获理学博士学位;1995年在加利福尼亚圣地亚哥完成博士后工作后, 曾任新加坡国立大学分子与细胞研究所高级研究员;香港科技大学助理教授和副教授(获终身职位), 现任厦门大学教授，生命科学学院院长。

　　摘要：Metabolic homeostasis is maintained by various cellular sensors, including the master kinases AMPK (AMP-activated protein kinase) and mTORC1. In response to low energy status, AMPK is activated to enhance catabolic activities with concurrent inhibition of anabolic processes such as fatty acid synthesis. In contrast, mTORC1 is activated when nutrients and growth factors are abundant. Previously, we discovered the mechanism by which AMP, as a low energy-charge signal, can autonomously initiate the assembly of an activating complex for AMPK in response to starvation. AMP binding causes a higher affinity of AMPK for the scaffold protein AXIN that also binds to LKB1, thereby promoting phosphorylation and activation of AMPK. More recently, we found most surprisingly that the late endosomal/lysosomal protein complex v-ATPase-Ragulator, essential for activation of mTORC1, is also required for AMPK activation. We also uncovered that AMPK is a residential protein of late endosome/lysosome. Under glucose starvation, the v-ATPase-Ragulator complex is accessible to AXIN/LKB1 for AMPK activation. Concurrently, mTORC dissociates from endosome and becomes inactivated. We have thus revealed a switch between catabolism and anabolism.

　　Most recently, we have uncovered other functions of ULK1/2 kinases than initiation of autophagy. We found that ULK1 functions to regulate glycolytic pathways by direct phosphorylation of multiple glycolytic enzymes. The functional outcome of the modulation of the enzymatic activities by ULK1 will be presented at the talk.

　　报告联系人：18M0组 朴海龙 （82463004）